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Biochemistry > Amino Acid Metabolism > Flashcards

Amino Acid Metabolism Flashcards

1
Q

The basic structural units of proteins are

A

amino acids

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2
Q

There are …. common amino acids found in proteins

A

20

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3
Q

What is an α carbon?

A

it is a tetrahedral carbon at the centre of an amino acid

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4
Q

Describe the basic amino acid structure

A
  • α-Carbon is chiral (except in glycine)
  • at pH of 7.0, uncharged amino acids are zwitterions
  • they have a tetrahedral structure
  • α-carbon is bonded to an amino group(NH2) and a carboxyl group(COOH) on the other side
  • a 3rd bond is always to H and the 4th bond is to a variable side chain(R)
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5
Q

6 properties of amino acids

A
  1. capacity to polymerize
  2. novel acid-base properties
  3. varies structure and chemical functionality
  4. chirality
  5. differ from each other by the R group
  6. R group influences solubility in water
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6
Q

The 5 main classes of the common amino acids based on the reactivities of their R groups

A
  1. Aliphatic non-polar
  2. Aromatic
  3. Polar uncharged
  4. Polar negatively charged
  5. Polar positively charged
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7
Q

Name all the aliphatic non-polar amino acids

Clue: GAVLIPM

A 
Glycine
Alanine
Valine
Leucine
Isoleucine
Proline
Methionine
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8
Q

Name the aromatic amino acids

Clue: PTT

A
  1. Phenylalanine
  2. Tryptophan
  3. Tyrosine
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9
Q

Name the polar uncharged amino acids

Clue: STCAG

A
  1. Serine
  2. Threonine
  3. Cysteine
  4. Asparagine
  5. Glutamine
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10
Q

Name the polar negatively charged amino acids

Clue: AG

A
  1. Aspartate

2. Glutamate

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11
Q

Name the polar positively charged amino acids

Clue: LAH

A
  1. Lysine
  2. Arginine
  3. Histidine
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12
Q

How are amino acids classified based on nutritional requirement?

A

Essential
Non-essential
Semi-essential

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13
Q

Name the essential amino acids

Clue: HILL MPT TV

A 
Histidine
Isoleucine
Leucine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
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14
Q

Name the non-essential amino acids

Clue: 4A C 3G PST

A 
Alanine
Arginine
Asparagine
Aspartate
Cysteine
Glycine
Glutamine
Glutamate
Proline
Serine
Tyrosine
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15
Q

Name the semi-essential amino acids

Clue: ACGGPT

A 
Arginine
Cysteine
Glutamine
Glycine
Proline
Tyrosine
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16
Q

When is Methionine produced in large amounts?

A

When cysteine is not adequately supplied in the diet, to produce cysteine

17
Q

When is Phenylalanine produced in large amounts?

A

when tyrosine is adequately supplied in the diet, it is needed to form tyrosine

18
Q

How are amino acids groups based on catabolic intermediates?

A

Glucogenic and Ketogenic

19
Q

What are glucogenic amino acids catabolized to?

A 
pyruvate
α-ketoglutarate
fumarate
succinyl CoA
oxaloacetate
20
Q

Examples of glucogenic amino acids

Clue: 4A C GH MPTV

A 
Alanine
Arginine
Asparagine
Aspartate
Glutamine
Histidine
Methionine
Proline
Threonine
Valine
21
Q

What are ketogenic amino acids catalyzed to?

A

acetyl CoA and acetoacetyl CoA

22
Q

Purely ketogenic amino acids

Clue: 2L

A

Leucine

Lysine

23
Q

Both glucogenic and ketogenic amino acids

Clue: IPTT

A

Isoleucine
Phenylalanine
Tryptophan
Tyrosine

24
Q

What are unusual amino acids?

A

they are formed from the modification of common amino acids

25
Q

3 examples of unusual amino acids

A

hydroxyproline
ornithine
norleucine

26
Q

What are the 4 general reactions of amino acids?

A
  1. Decarboxylation
  2. Transamination
  3. Oxidative deamination
  4. Transdeamination
27
Q

Amino acids are decarboxylated to form ……….

A

amines.
eg. 1. Histamine from Histidine
2. L-Dopa from Tyrosine
3. Serotonin from Tryptophan

28
Q

What is transamination?

A

transfer of amino group from an amino acid to an α-keto-acid to from the corresponding amino acid

29
Q

What enzyme catalyzes transamination and what prosthetic group does it require?

A

amino transferases

requires pyridoxal phosphate (PLP), a derivative of vitamin B6

30
Q

What’s the function of PLP?

A

it is an intermediate carrier of the amino groups at the active site of amino transferase

31
Q

What type of transformation does PLP undergo?

A

reversible transformation between the aldehyde form and the aminated form, pyridoxamine phosphate

32
Q

In mammals, which amino acids can’t be transaminated?

A

Lysine

Threonine

33
Q

What type of reaction can’t proline participate in and why?

A

PLP dependent reactions including transamination and decarboxylation
because it has a secondary amino group

34
Q

Where does oxidative deamination of glutamate occur?

A

mitochondria of the liver cells

35
Q

What are the products of oxidative deamination of glutamate and which enzyme catalyzes the reaction?

A

α-ketoglutarate and ammonium ions

glutamate dehydrogenase is the enzyme

36
Q

When does glutamate dehydrogenase activity increase?

A

when hepatocytes require fuel from TCA

37
Q

What are the allosteric activators and inhibitors of glutamate dehydrogenase?

A

AA- GDP& ADP

AI- GTP&ATP

38
Q

What is transdeamination?

A

the combined action of amino transferases and glutamate dehydrogenase

39
Q

What does the coupling of oxidative deamination and transamination do?

A

creates an avenue for deaminating all amino acids

Biochemistry (9 decks)

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